ID A0A1M6KDJ0_9CLOT Unreviewed; 426 AA.
AC A0A1M6KDJ0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Gamma-D-glutamyl-(L)-meso-diaminopimelate peptidase I. Metallo peptidase. MEROPS family M14C {ECO:0000313|EMBL:SHJ57009.1};
GN ORFNames=SAMN02745248_00430 {ECO:0000313|EMBL:SHJ57009.1};
OS Hathewaya proteolytica DSM 3090.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX NCBI_TaxID=1121331 {ECO:0000313|EMBL:SHJ57009.1, ECO:0000313|Proteomes:UP000183952};
RN [1] {ECO:0000313|EMBL:SHJ57009.1, ECO:0000313|Proteomes:UP000183952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3090 {ECO:0000313|EMBL:SHJ57009.1,
RC ECO:0000313|Proteomes:UP000183952};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; FRAD01000004; SHJ57009.1; -; Genomic_DNA.
DR RefSeq; WP_072901808.1; NZ_FRAD01000004.1.
DR AlphaFoldDB; A0A1M6KDJ0; -.
DR STRING; 1121331.SAMN02745248_00430; -.
DR OrthoDB; 9811296at2; -.
DR Proteomes; UP000183952; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd06229; M14_Endopeptidase_I; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034274; ENP1_M14_CPD.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000183952}.
FT DOMAIN 73..117
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 426 AA; 48267 MW; 85A9259A8564CFC4 CRC64;
MIILKENDRG NKVSKLQSIL RQLKFYKEPV DGIFGAKTKE AVINFQKSNG LLDTGIVDDL
TMDAIDRYRN GYFIYSVEKG DTLSGIGEKY GVSLQQLVMI NKLEDDSILT IGQELIIPYP
GINIVPTDVK YDYEVLERNI KSLKVLYPFL QVGTIGESVL GKKMYYLRLG TGEKEVGYNG
AHHAIEWITS TFLMKFIEEF SKVYSKKQEF FGYSPEKIWN EASMYIVPMV NPDGVDLVIN
GVEESNPYYD KLIKWNKGSK DFSTTWSANI RGVDLNHNYD ASFEESKKAE ESYGVFGPGP
TRYGGPYPQS EPESNNLVNF TREHDFRLVL AYHSQGEVIY WQYLDEAPQE ALPIGETFAK
ISGYSLSETT GITSFAGYKD WFIKEFNRPG YTVEVGLGKN PLPLSQICEI YRDNAGVLME
AAIITE
//